Reversible mechanochemical engines comprised of bioelastomers capable of modulable inverse temperature transitions for the interconversion of chemical and mechanical work

Claim 2

A mechanochemical engine capable of converting chemical work to mechanical work, which comprises: an elastomeric material capable of reversibly contracting and relaxing by an inverse temperature transition upon changing chemical potential of a surrounding medium; means for changing the chemical potential of said surrounding medium; and means for converting contracting or relaxing of said elastomeric material into mechanical work.

Claim 3

The mechanochemical engine of claim 1, wherein said elastomeric material comprises a bioelastomer which contains elastomeric units comprising tetrapeptide or pentapeptide repeating units or mixtures thereof, wherein said repeating units comprise amino acid residues selected from the group consisting of hydrophobic amino acid and glycine residues and said repeating units exist in a conformation having a β-turn.

Claim 4

The mechanochemical engine of claim 2, wherein said means for changing the chemical potential of said surrounding medium comprises a first salt solution and a second salt solution, wherein said first and second salt solutions differ in concentration by at least 0.02N.

Claim 5

The mechanochemical engine of claim 3, wherein said means for converting or contracting or relaxing of said elastomeric material into mechanical work comprises: a) a first pulley, attached to b) three concentric pulleys with said pulleys sharing a common axis; and c) a second pulley, attached also to said three pulleys; wherein said first pulley is immersed in said first salt solution and said second pulley is immersed in said second salt operation.

Claim 6

The mechanochemical engine of claim 2, wherein said repeating unit having a β-turn comprises a polypentapeptide unit of formula: --X.sup.1 --(IPGVG).sub.n --Y.sup.1 -- wherein: I is a peptide-forming residue of L-isoleucine; P is a peptide-forming residue of L-proline; G is a peptide-forming residue of glycine; V is a peptide-forming residue of L-valine; and wherein X 1 is PGVG, GVG, VG, G, or a covalent bond; Y 1 is IPGV, IPG, IP, or I, or a covalent bond; and n is an integer from 1 to 200.

Claim 7

The mechanochemical engine of claim 2, wherein said repeating unit having a β-turn comprises a polypentapeptide unit of formula: --X.sup.1 --(IPGVG).sub.n --Y.sup.1 -- and a polypentapeptide unit of formula: --X.sup.2 --(VPGVG).sub.n --Y.sup.2 -- wherein: I is a peptide-forming residue of L-isoleucine; P is a peptide-forming residue of L-proline; G is a peptide-forming residue of glycine; V is a peptide-forming residue of L-valine; and wherein each of X 1 and X 2 is PGVG, GVG, G, or a covalent bond; Y 1 is IPGV, IPG, IP, or I, or a covalent bond; Y 2 is VPGV, VPG, VP, or V, or a covalent bond; and each n independently is an integer from 1 to 200.

Claim 8

The mechanochemical engine of claim 2, wherein said repeating unit having a β-turn comprises a polypentapeptide unit of formula: --X.sup.1 --(IPGVG).sub.n --Y.sup.1 -- and a polypentapeptide unit for formula: --X.sup.2 --(VPGVG).sub.n --Y.sup.2 -- or a polytetrapeptide unit of formula: --X.sup.3 --(VPG).sub.n --Y.sup.3 -- or --X.sup.4 --(IPGG).sub.n --Y.sup.4 -- wherein: I is a peptide-forming residue of L-isoleucine; P is a peptide-forming residue of L-proline; G is a peptide-forming residue of glycine; V is a peptide-forming residue of L-valine; and wherein each of X 1 and X 2 is PGVG, GVG, VG, G, or a covalent bond; Y 1 is IPGV, IPG, IP, or I, or a covalent bond; Y 2 is VPGV, VPG, VP, or V, or a covalent bond; each of X 3 and X 4 is PGG, GG, G, or a covalent bond; Y 3 is VPG, VP, V, or a covalent bond; Y 4 is IPG, IP, I, or a covalent bond; and each n independently is an integer from 1 to 200.

Claim 9

The mechanochemical engine of claim 2, wherein said elastomeric material comprises cross-linked bioelastomer.

Claim 10

The mechanochemical engine of claim 8, wherein said bioelastomer is cross-linked by γ-irradiation.

Claim 11

The mechanochemical engine of claim 2, wherein said repeating unit having a β-turn comprises a polypentapeptide unit of formula: --(αPρΩG).sub.n -- wherein: P is a peptide-forming residue of L-proline; G is a peptide-forming residue of glycine; α is a peptide-forming residue of L-valine or selected from the group consisting of L--Glu, L--Asp, L--His, L--Lys, L--Tyr, and other ionizable L-amino acid residue; ρ is a peptide-forming residue of glycine or selected from the group consisting of D--Glu, D--Asp, D--His, D--Lys, and D--Tyr, and other ionizable peptide-forming D-amino acid residues; Ω is a peptide-forming residue of L-valine or selected from the group consisting of L--Glu, L--Asp, L--His, L--Lys, L--Tyr, and other ionizable L-amino acid residues; and n is an integer from 1 to 5,000.

Claim 12

The mechanochemical engine of claim 10, wherein in at least one said pentapeptide repeating unit, at least one of said α or Ω or ρ is an ionizable amino acid residue.

Claim 13

The mechanochemical engine of claim 2, wherein said repeating unit having the β-turn comprises a polypentapeptide unit of formula: --(VPφδ).sub.n -- wherein P is a peptide-forming residue of L-proline; V is a peptide-forming residue of L-valine; φ is a peptide-forming residue selected from the group consisting of D--Glu, D--Asp, D--His, D--Lys, and D--Tyr, and other ionizable peptide-forming D-amino acid residues; δ is a peptide-forming residue selected from the group consisting of L--Glu, L--Asp, L--His, L--Lys, L--Tyr, and other ionizable L-amino acid residues; and n is an integer from 1 to 5,000.

Claim 14

The mechanochemical engine of claim 12, wherein in at least one said pentapeptide repeating unit, at least one of said φ or δ is an ionizable amino acid residue.

Claim 15

A mechanochemical engine capable of converting chemical work to mechanical work, which comprises: an elastomeric material capable of reversibly contracting and relaxing by an inverse temperature transition upon changing between a fist sate of chemical functionality and a second state of chemical functionality of said elastomeric material, wherein a change between a first composition and a second composition of a medium surrounding said elastomeric material is capable of changing chemical functionality between said first state and said second state; means for changing said medium surrounding said elastomeric material from said first composition to said second composition; and means for converting contracting or relaxing of said elastomeric material into mechanical work.

Claim 16

A mechanochemical engine capable of converting chemical work to mechanical work, which comprises: an elastomeric material capable of reversibly contracting and relaxing by an inverse temperature transition upon changing between a fist sate of chemical functionality and a second state of chemical functionality of said elastomeric material, wherein a change between a first composition and a second composition of a medium surrounding said elastomeric material is capable of changing chemical functionality between said first state and said second state; means for changing said medium surrounding said elastomeric material from said first composition to said second composition; and means for converting contracting or relaxing of said elastomeric material into mechanical work.

Claim 17

The mechanochemical engine of claim 14, wherein said first and second states differ in chemical potential by at least 0.05 kcal/mole of said chemical functionality.

Claim 18

The mechanochemical engine of claim 13, wherein said elastomeric material comprises a bioelastomer which contains elastomeric units comprising tetrapeptide or pentapeptide repeating units, or mixtures thereof, wherein said repeating units comprise amino acid residues selected from the group consisting of hydrophobic amino acid and glycine residues, wherein said repeating units exist in a conformation having a β-turn.

Claim 19

The mechanochemical engine of claim 16, wherein said repeating unit having a β-turn comprises a polypentapeptide unit of formula: --(αPρΩG).sub.n -- wherein: P is a peptide-forming residue of L-proline; G is a peptide-forming residue of glycine; α is a peptide-forming residue of L-valine or selected from the group consisting of L--Glu, L--Asp, L--His, L--Lys, L--Tyr, and other ionizable L-amino acid residues; ρ is a peptide-forming residue of glycine or selected from the group consisting of D--Glu, D--Asp, D--His, D--Lys, and D--Tyr, and other ionizable peptide-forming D-amino acid residues; Ω is a peptide-forming residue of L-valine or selected from the group consisting of L--Glu, L--Asp, L--His, L--Lys, L--Tyr, and other ionizable L-amino acid residues; and n is an integer from 1 to 5,000.

Claim 20

The mechanochemical engine of claim 17, wherein in at least one of said pentapeptide repeating unit, at least one of said α or Ω or ρ is an ionizable amino acid residue.

Claim 21

The mechanochemical engine of claim 16, wherein said repeating unit having a β-turn comprises a polypentapeptide unit of formula: --(VPφδ).sub.n -- wherein: P is a peptide-forming residue of L-proline; V is a peptide-forming residue of L-valine; φ is a peptide-forming residue selected from the group consisting of D--Glu, D--Asp, D--His, D--Lys, and D--Tyr, and other ionizable peptide-forming D-amino acid residues; δ is a peptide-forming residue selected from the group consisting of L--Glu, L--Asp, L--His, L--Lys, L--Tyr, and other ionizable L-amino acid residues; and n is an integer from 1 to 5,000.

Claim 22

The mechanochemical engine of claim 19, wherein in at least one said pentapeptide repeating unit, at least one of said φ or δ is an ionizable amino acid residue.

Claim 23

The mechanochemical engine of claim 16, wherein said elastomeric material comprises cross-linked bioelastomer.

Claim 24

The mechanochemical engine of claim 21, wherein said bioelastomer is cross-linked by γ-irradiation.

Claim 25

The mechanochemical engine of claim 16, wherein said elastomeric material comprises 20%--Glu 4 --PPP.

Claim 26

The mechanochemical engine of claim 16, wherein said chemical functionality comprises carboxylic acid.

Claim 27

The mechanochemical engine of claim 24, wherein said carboxylic acid is present on an amino acid residue selected from the group consisting of D--Glu, L--Glu, homologues of D-- or L--Glu having additional --CH 2 -- groups in the side chain, and homologues of D-- or L--Glu having additional --CO 2 --groups in the side chain.

Claim 28

The mechanochemical engine of claim 16, wherein said change between a first composition and a second composition of a medium comprises a change in pH of said medium.

Claim 29

The mechanochemical engine of claim 16, wherein said change between a first composition and a second composition of a medium comprises a change in concentration of Ca +2 .

Claim 30

The mechanochemical engine of claim 16, wherein said changing between said first state of chemical functionality and said second state of chemical functionality comprises phosphorylation-dephosphorylation.

Claim 31

The mechanochemical engine of claim 16, wherein said changing between said first state of chemical functionality and said second state of chemical functionality comprises amidation-deamidation.